==== Secondary Structure Definition by the program DSSP, updated CMBI version by ElmK / April 1,2000 ==== DATE=3-DEC-2009 . REFERENCE W. KABSCH AND C.SANDER, BIOPOLYMERS 22 (1983) 2577-2637 . HEADER PROTEASE INHIBITOR 02-APR-01 1HA9 . COMPND 2 MOLECULE: TRYPSIN INHIBITOR II; . SOURCE 2 ORGANISM_SCIENTIFIC: MOMORDICA COCHINCHINENSIS; . AUTHOR A.HEITZ,J.-F.HERNANDEZ,J.GAGNON,T.T.HONG,T.T.C.PHAM, . 34 1 3 3 0 TOTAL NUMBER OF RESIDUES, NUMBER OF CHAINS, NUMBER OF SS-BRIDGES(TOTAL,INTRACHAIN,INTERCHAIN) . 2612.0 ACCESSIBLE SURFACE OF PROTEIN (ANGSTROM**2) . 17 50.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(J) , SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS IN PARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 6 17.6 TOTAL NUMBER OF HYDROGEN BONDS IN ANTIPARALLEL BRIDGES, SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-5), SAME NUMBER PER 100 RESIDUES . 1 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-4), SAME NUMBER PER 100 RESIDUES . 1 2.9 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-3), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-2), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I-1), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+0), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+1), SAME NUMBER PER 100 RESIDUES . 5 14.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+2), SAME NUMBER PER 100 RESIDUES . 5 14.7 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+3), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+4), SAME NUMBER PER 100 RESIDUES . 0 0.0 TOTAL NUMBER OF HYDROGEN BONDS OF TYPE O(I)-->H-N(I+5), SAME NUMBER PER 100 RESIDUES . 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 *** HISTOGRAMS OF *** . 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 RESIDUES PER ALPHA HELIX . 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 PARALLEL BRIDGES PER LADDER . 3 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 ANTIPARALLEL BRIDGES PER LADDER . 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 LADDERS PER SHEET . # RESIDUE AA STRUCTURE BP1 BP2 ACC N-H-->O O-->H-N N-H-->O O-->H-N TCO KAPPA ALPHA PHI PSI X-CA Y-CA Z-CA 1 1 A S 0 0 27 0, 0.0 24,-0.2 0, 0.0 6,-0.1 0.000 360.0 360.0 360.0 126.7 3.1 1.9 -1.5 2 2 A G - 0 0 28 22,-1.5 2,-2.3 4,-0.2 23,-0.1 0.410 360.0-147.9 -93.8 -1.9 0.9 2.6 -4.7 3 3 A S B > S+A 6 0A 96 3,-0.7 3,-1.5 21,-0.3 -1,-0.1 -0.203 83.5 79.1 64.2 -42.9 1.6 6.4 -4.2 4 4 A D T 3 S+ 0 0 167 -2,-2.3 -1,-0.2 1,-0.3 3,-0.1 0.806 97.4 44.7 -62.8 -30.7 -1.8 7.5 -5.7 5 5 A G T 3 S- 0 0 59 19,-0.4 -1,-0.3 1,-0.4 2,-0.2 0.342 128.6 -92.5 -89.4 1.6 -3.5 6.7 -2.3 6 6 A G B < -A 3 0A 34 -3,-1.5 2,-0.7 18,-0.2 -3,-0.7 -0.619 65.1 -35.1 113.5-175.1 -0.7 8.4 -0.3 7 7 A V - 0 0 129 -2,-0.2 17,-0.2 -5,-0.1 18,-0.1 -0.760 58.8-151.7 -78.9 112.5 2.6 7.2 1.3 8 8 A a - 0 0 0 -2,-0.7 -2,-0.1 16,-0.3 15,-0.0 -0.728 20.4-126.8 -79.9 139.6 2.1 3.7 2.6 9 9 A P - 0 0 115 0, 0.0 -1,-0.1 0, 0.0 -2,-0.0 0.512 42.5-130.8 -55.2 -8.2 4.4 2.6 5.7 10 10 A K - 0 0 128 1,-0.1 2,-0.2 12,-0.1 24,-0.1 0.930 31.7-172.1 51.8 64.8 5.4 -0.4 3.5 11 11 A I - 0 0 79 1,-0.1 2,-1.2 2,-0.0 22,-0.2 -0.558 34.0-116.1 -78.8 147.9 4.9 -3.4 5.9 12 12 A L + 0 0 155 -2,-0.2 2,-0.6 20,-0.1 -1,-0.1 -0.179 61.9 147.4 -80.7 42.5 6.1 -6.9 4.8 13 13 A K - 0 0 102 -2,-1.2 20,-2.7 20,-0.1 2,-0.1 -0.751 44.5-136.7 -79.5 113.2 2.5 -8.3 4.9 14 14 A K B +B 32 0B 151 -2,-0.6 18,-0.3 18,-0.3 2,-0.3 -0.476 33.6 178.6 -66.0 145.4 2.0 -11.0 2.2 15 15 A b - 0 0 23 16,-2.6 3,-0.1 -2,-0.1 -1,-0.0 -0.881 44.6-153.9-144.8 171.6 -1.3 -10.6 0.3 16 16 A R S S+ 0 0 221 1,-0.4 2,-0.3 -2,-0.3 -1,-0.1 0.534 87.9 7.1-119.7 -28.5 -3.7 -11.9 -2.5 17 17 A R S > S- 0 0 124 14,-0.1 3,-1.4 9,-0.0 -1,-0.4 -0.929 80.6 -96.8-149.3 173.2 -5.4 -8.5 -3.2 18 18 A D G > S+ 0 0 63 -2,-0.3 3,-1.3 1,-0.3 7,-0.1 0.778 115.7 68.8 -66.1 -27.1 -5.3 -4.8 -2.3 19 19 A S G 3 S+ 0 0 118 1,-0.3 -1,-0.3 8,-0.1 4,-0.1 0.677 91.3 62.7 -66.4 -19.8 -8.0 -5.3 0.4 20 20 A D G < S+ 0 0 57 -3,-1.4 -1,-0.3 2,-0.1 -2,-0.2 0.732 96.6 76.5 -70.0 -25.3 -5.4 -7.3 2.4 21 21 A c S < S- 0 0 18 -3,-1.3 6,-0.1 -4,-0.3 -7,-0.0 -0.489 87.1 -98.8 -96.3 157.3 -3.2 -4.1 2.7 22 22 A P > - 0 0 51 0, 0.0 3,-2.1 0, 0.0 -1,-0.1 -0.294 59.6 -68.8 -71.3 161.4 -3.3 -0.9 4.9 23 23 A G T 3 S+ 0 0 88 1,-0.3 -15,-0.1 -4,-0.1 -2,-0.1 0.516 126.4 23.1 -12.3 -75.1 -4.8 2.4 3.6 24 24 A A T 3 S+ 0 0 19 -17,-0.2 -22,-1.5 2,-0.0 -19,-0.4 0.498 104.9 95.8 -89.5 -8.6 -2.3 3.8 1.0 25 25 A a < - 0 0 11 -3,-2.1 2,-0.3 -24,-0.2 -4,-0.1 -0.333 53.7-157.8 -74.5 166.4 -0.7 0.4 0.0 26 26 A I - 0 0 59 8,-2.7 8,-1.9 6,-0.1 2,-1.0 -0.876 35.1 -98.5-128.9 162.2 -1.5 -2.0 -2.9 27 27 A b B -C 33 0C 13 -2,-0.3 6,-0.2 6,-0.2 -9,-0.2 -0.804 52.1-145.6 -86.2 100.1 -0.9 -5.7 -3.3 28 28 A R > - 0 0 135 4,-2.4 3,-1.9 -2,-1.0 4,-0.2 -0.025 25.1 -94.5 -65.1 171.1 2.3 -5.5 -5.5 29 29 A G T 3 S+ 0 0 93 1,-0.3 -1,-0.1 2,-0.1 -2,-0.0 0.650 121.4 61.9 -68.6 -17.3 3.4 -8.0 -8.3 30 30 A N T 3 S- 0 0 116 2,-0.2 -1,-0.3 3,-0.0 3,-0.1 0.411 120.9-103.1 -84.9 -2.7 5.6 -10.0 -5.8 31 31 A G S < S+ 0 0 27 -3,-1.9 -16,-2.6 1,-0.3 2,-0.3 0.705 88.2 100.9 85.0 22.7 2.5 -11.0 -3.7 32 32 A Y B S-B 14 0B 85 -18,-0.3 -4,-2.4 -4,-0.2 -1,-0.3 -0.918 76.7 -93.4-131.0 159.8 3.2 -8.5 -0.8 33 33 A c B C 27 0C 12 -20,-2.7 -6,-0.2 -2,-0.3 -20,-0.1 -0.433 360.0 360.0 -69.4 145.6 1.9 -5.1 0.3 34 34 A G 0 0 9 -8,-1.9 -8,-2.7 -2,-0.1 -32,-0.2 -0.970 360.0 360.0-167.5 360.0 3.7 -1.9 -0.8